2024
Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex
Chavali S, Chou S, Cao W, Pollard T, De La Cruz E, Sindelar C. Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications 2024, 15: 2059. PMID: 38448439, PMCID: PMC10918085, DOI: 10.1038/s41467-024-46179-x.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin-Related Protein 2-3 ComplexActinsCryoelectron MicroscopyCytoskeletonPhosphatesConceptsArp2/3 complexActin filamentsCryo-EM structureMother filamentDaughter filamentArp2/3 complex nucleates branched actin filamentsActin filament branchingBranched actin filamentsDissociation of PiADP-PiFilament branchingOrganelle movementADP stateBranch junctionsArp3A-resolutionActinArp2/3ADP-BeFxFilamentsADPPhosphate releaseFilament mechanismArp2Organelles
2022
The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release
Gray S, Cao W, Montpetit B, De La Cruz EM. The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release. Nucleic Acids Research 2022, 50: 3998-4011. PMID: 35286399, PMCID: PMC9023272, DOI: 10.1093/nar/gkac164.Peer-Reviewed Original ResearchConceptsNuclear pore complexRNA exportDEAD-box protein Dbp5ATPase cycleDbp5's ATPase activityDEAD (Asp-Glu-Ala-Asp) box protein 5Pore complexDbp5ATP bindingATPase cyclingNucleotide stateCytoplasmic faceGle1Pool of ATPADP-PiGene expressionProtein 5Mechanistic understandingNucleoporinsNup159ATPase activityATP dissociationATPPi releasePi release rate
2020
Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches
Pandit NG, Cao W, Bibeau J, Johnson-Chavarria EM, Taylor EW, Pollard TD, De La Cruz EM. Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 13519-13528. PMID: 32461373, PMCID: PMC7306818, DOI: 10.1073/pnas.1911183117.Peer-Reviewed Original ResearchConceptsActin filament branchesArp2/3 complexMother filamentFilament branchesTotal internal reflection fluorescence microscopyEssential cellular functionsMechanical forcesActin filament networkReflection fluorescence microscopyCellular functionsActin networkCell motilityComplex generatesActin filamentsArp2/3Filament networkFluorescence microscopyState 1Branch junctionsState 2FilamentsComplexesPhosphate releaseMuscle actinADP
2018
Insights into the Cooperative Nature of ATP Hydrolysis in Actin Filaments
Katkar HH, Davtyan A, Durumeric AEP, Hocky GM, Schramm AC, De La Cruz EM, Voth GA. Insights into the Cooperative Nature of ATP Hydrolysis in Actin Filaments. Biophysical Journal 2018, 115: 1589-1602. PMID: 30249402, PMCID: PMC6260209, DOI: 10.1016/j.bpj.2018.08.034.Peer-Reviewed Original Research
2015
Pi Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5)
Wong EV, Cao W, Vörös J, Merchant M, Modis Y, Hackney DD, Montpetit B, De La Cruz EM. Pi Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5). Journal Of Molecular Biology 2015, 428: 492-508. PMID: 26730886, PMCID: PMC4744555, DOI: 10.1016/j.jmb.2015.12.018.Peer-Reviewed Original Research
2007
The ATPase Cycle Mechanism of the DEAD-box rRNA Helicase, DbpA
Henn A, Cao W, Hackney DD, De La Cruz EM. The ATPase Cycle Mechanism of the DEAD-box rRNA Helicase, DbpA. Journal Of Molecular Biology 2007, 377: 193-205. PMID: 18237742, PMCID: PMC2359651, DOI: 10.1016/j.jmb.2007.12.046.Peer-Reviewed Original ResearchFluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates
Zhang H, Cao W, Zakharova E, Konigsberg W, De La Cruz EM. Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates. Nucleic Acids Research 2007, 35: 6052-6062. PMID: 17766250, PMCID: PMC2094073, DOI: 10.1093/nar/gkm587.Peer-Reviewed Original ResearchConceptsHydroxyl groupsNucleotidyl transfer reactionMinimal kinetic schemeConformational changesDetectable fluorescence changeChemical quenchTransfer reactionsDependent fluorescence enhancementFluorescence enhancementFluorescence quenchingFluorescent probeRapid conformational changesTemplate complexN-positionRate constantsFluorescence changesRapid fluorescenceTernary complexKinetic schemeComplexesTemplating baseDependent conformational changesDp/TTemplateFluorescence
2001
Structural biology. Actin' up.
De La Cruz E, Pollard T. Structural biology. Actin' up. Science 2001, 293: 616-8. PMID: 11474090, DOI: 10.1126/science.1063558.Peer-Reviewed Original ResearchActin Depolymerizing FactorsActinsAdenosine DiphosphateAdenosine TriphosphateBiopolymersContractile ProteinsCrystallography, X-RayHydrolysisMicrofilament ProteinsPhosphatesProfilinsProtein BindingProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsRhodaminesThymosin
1999
The kinetic mechanism of myosin V
De La Cruz E, Wells A, Rosenfeld S, Ostap E, Sweeney H. The kinetic mechanism of myosin V. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 13726-13731. PMID: 10570140, PMCID: PMC24132, DOI: 10.1073/pnas.96.24.13726.Peer-Reviewed Original Research
1994
Transient kinetic analysis of rhodamine phalloidin binding to actin filaments.
De La Cruz EM, Pollard TD. Transient kinetic analysis of rhodamine phalloidin binding to actin filaments. Biochemistry 1994, 33: 14387-92. PMID: 7981198, DOI: 10.1021/bi00252a003.Peer-Reviewed Original Research